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Database: UniProt
Entry: A0A2U2AF54_9GAMM
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ID   A0A2U2AF54_9GAMM        Unreviewed;       242 AA.
AC   A0A2U2AF54;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   RecName: Full=2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase {ECO:0000256|HAMAP-Rule:MF_00108};
DE            EC=2.7.7.60 {ECO:0000256|HAMAP-Rule:MF_00108};
DE   AltName: Full=4-diphosphocytidyl-2C-methyl-D-erythritol synthase {ECO:0000256|HAMAP-Rule:MF_00108};
DE   AltName: Full=MEP cytidylyltransferase {ECO:0000256|HAMAP-Rule:MF_00108};
DE            Short=MCT {ECO:0000256|HAMAP-Rule:MF_00108};
GN   Name=ispD {ECO:0000256|HAMAP-Rule:MF_00108};
GN   ORFNames=DC083_05190 {ECO:0000313|EMBL:PWD81285.1};
OS   Ignatzschineria ureiclastica.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Cardiobacteriales;
OC   Ignatzschineriaceae; Ignatzschineria.
OX   NCBI_TaxID=472582 {ECO:0000313|EMBL:PWD81285.1, ECO:0000313|Proteomes:UP000245020};
RN   [1] {ECO:0000313|Proteomes:UP000245020}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KCTC 22644 {ECO:0000313|Proteomes:UP000245020};
RA   Tsang C.C., Tang J.Y.M., Fong J.Y.H., Kinne J., Lee H.H., Joseph M.,
RA   Jose S., Schuster R.K., Tang Y., Sivakumar S., Chen J.H.K., Teng J.L.L.,
RA   Lau S.K.P., Wernery U., Woo P.C.Y.;
RT   "Ignatzschineria dubaiensis sp. nov., isolated from necrotic foot tissues
RT   of dromedaries (Camelus dromedarius) and associated maggots in Dubai,
RT   United Arab Emirates.";
RL   Submitted (MAY-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the formation of 4-diphosphocytidyl-2-C-methyl-D-
CC       erythritol from CTP and 2-C-methyl-D-erythritol 4-phosphate (MEP).
CC       {ECO:0000256|ARBA:ARBA00002459, ECO:0000256|HAMAP-Rule:MF_00108}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-C-methyl-D-erythritol 4-phosphate + CTP + H(+) = 4-CDP-2-C-
CC         methyl-D-erythritol + diphosphate; Xref=Rhea:RHEA:13429,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:37563,
CC         ChEBI:CHEBI:57823, ChEBI:CHEBI:58262; EC=2.7.7.60;
CC         Evidence={ECO:0000256|ARBA:ARBA00001282, ECO:0000256|HAMAP-
CC         Rule:MF_00108};
CC   -!- PATHWAY: Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis
CC       via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-
CC       phosphate: step 2/6. {ECO:0000256|ARBA:ARBA00004787, ECO:0000256|HAMAP-
CC       Rule:MF_00108}.
CC   -!- SIMILARITY: Belongs to the IspD/TarI cytidylyltransferase family. IspD
CC       subfamily. {ECO:0000256|ARBA:ARBA00009789, ECO:0000256|HAMAP-
CC       Rule:MF_00108}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:PWD81285.1}.
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DR   EMBL; QEWQ01000003; PWD81285.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2U2AF54; -.
DR   OrthoDB; 9806837at2; -.
DR   UniPathway; UPA00056; UER00093.
DR   Proteomes; UP000245020; Unassembled WGS sequence.
DR   GO; GO:0050518; F:2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0019288; P:isopentenyl diphosphate biosynthetic process, methylerythritol 4-phosphate pathway; IEA:UniProtKB-UniPathway.
DR   GO; GO:0016114; P:terpenoid biosynthetic process; IEA:UniProtKB-UniRule.
DR   CDD; cd02516; CDP-ME_synthetase; 1.
DR   HAMAP; MF_00108; IspD; 1.
DR   InterPro; IPR001228; IspD.
DR   InterPro; IPR034683; IspD/TarI.
DR   InterPro; IPR018294; ISPD_synthase_CS.
DR   InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR   NCBIfam; TIGR00453; ispD; 1.
DR   PANTHER; PTHR32125; 2-C-METHYL-D-ERYTHRITOL 4-PHOSPHATE CYTIDYLYLTRANSFERASE, CHLOROPLASTIC; 1.
DR   PANTHER; PTHR32125:SF4; 2-C-METHYL-D-ERYTHRITOL 4-PHOSPHATE CYTIDYLYLTRANSFERASE, CHLOROPLASTIC; 1.
DR   Pfam; PF01128; IspD; 1.
DR   SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1.
DR   PROSITE; PS01295; ISPD; 1.
PE   3: Inferred from homology;
KW   Isoprene biosynthesis {ECO:0000256|ARBA:ARBA00023229, ECO:0000256|HAMAP-
KW   Rule:MF_00108};
KW   Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695, ECO:0000256|HAMAP-
KW   Rule:MF_00108}; Reference proteome {ECO:0000313|Proteomes:UP000245020};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_00108}.
FT   SITE            22
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00108"
FT   SITE            29
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00108"
FT   SITE            167
FT                   /note="Positions MEP for the nucleophilic attack"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00108"
FT   SITE            223
FT                   /note="Positions MEP for the nucleophilic attack"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00108"
SQ   SEQUENCE   242 AA;  26550 MW;  3379577AF8B2357B CRC64;
     MVEKVAIPEI YFVIPAAGVG SRMGADCPKQ YLMLAGKSVL YHTLSLFLSV DAIAGGVVVR
     SQGDPTPLPL ESERLWETIG GETRTESVTA GLQYLANRLS KAGKSLDDVW VLVHDAARPG
     LKSSELALFC DHLVSTQPEA GLIMAMPAQD TVKRADETGR VIRTEDRSTL WLAQTPQAAK
     LGVLLNASEK ILRDGVNVTD EASILEYNGL FPQLYRGYSH NLKITYPEDL ELMRLYFTAR
     EV
//
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